Recombinant Mouse Neurofilament Light Polypeptide (NEFL)

Name: Recombinant Mouse Neurofilament Light Polypeptide (NEFL)
Brand: Beta LifeScience
SKU: BLC-00325P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Neurofilament Light Polypeptide (NEFL) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P08551
Target Symbol	NEFL
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	SSFGYDPYFSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYSGLQSSSYLMSARSFPAYYTSHVQEEQTEVEETIEATKAEEAKDEPPSEGEAEEEEKEKEEGEEEEGAEEEEAAKDESEDTKEEEEGGEGEEEDTKESEEEEKKEESAGEEQVAKKKD
Expression Range	2-543aa
Protein Length	Full Length of Mature Protein
Mol. Weight	61.5 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks.
Subcellular Location	Cell projection, axon. Cytoplasm, cytoskeleton.
Protein Families	Intermediate filament family
Database References	KEGG: mmu:18039 STRING: 10090.ENSMUSP00000022639 UniGene: PMID: 27021905 It may have a role in protecting neurites from dystrophy and in regulating cellular pathways related to the generation of Ab plaques. PMID: 26344875 Nefl(N98S/+) mice had a noticeable tremor, and most animals showed a hindlimb clasping similar to human Charcot-Marie-Tooth Type 2E phenotype. PMID: 25552649 Mice lacking NF-Lr ecapitulated the delayed synapse elimination phenotype observed in micelacking Nfasc155. PMID: 25232125 The finding of this study suggested that a lack of NFL protein alters the expression of cytoskeletal proteins and disrupts other NF subunits, causing intracellular aggregation but not gross structural changes in cortical neurons or cytoarchitecture. PMID: 23172043 Neurofilament light chain (NFL) and neuronal intermediate filament protein alpha-internexin accumulate in axon swellings in the spinal white matter in a superoxide dismutase (SOD)-1 mouse model. PMID: 22609817 Data suggest that tetrahydropapaveroline (an endogenous catechol) causes oxidative stress resulting in astrocyte/neuronal cell death via generation of reactive oxygen species and modification/aggregation of NF-L (as in neurodegenerative diseases). PMID: 23228886 Data show that mitochondria essentially stopped moving in neurons expressing neurofilament protein (NFL) mutants, probably a consequence of cytoskeletal disruption. PMID: 22155564 NEFL transgenic mice exhibited extended duration of the hindlimb clasping response and gait anomalies, as well as sensorimotor deficits in stationary beam and suspended bar tests PMID: 21168446 Neuropathic effects of overexpressing NF-L can occur at the level of transgene RNA and are mediated by sequences in the NF-L 3' UTR PMID: 12196589 nNOS inhibitor, AR-R17477AR, prevents the loss of NF68 immunoreactivity induced by methamphetamine in the mouse striatum PMID: 12675928 The 3' untranslated region of light neurofilament (NF-L) transcript enhances the reactivity of its own translated product and leads to loss of solubility and aggregation of NF-L protein and to coaggregation of mutant superoxide dismutase 1 (SOD1) protein PMID: 15028764 copper-mediated NF-L modification may be closely related to oxidative reactions which play a critical role in neurodegenerative diseases PMID: 15388232 We observed three overlapping phases in NF-L transgenic mice, including transient aggregate formation, reactive microgliosis, and progressive motor neuron loss. PMID: 15920739 p190RhoGEF is involved in aggregation of NF-L protein and support a working hypothesis that aggregation of p190RhoGEF and NF-L is an upstream event triggering neurotoxicity in motor neuron disease. PMID: 16236762 Mouse lactotrophs, gonadotrophs, thyrotrophs and somatotrophs express NF68 in a sexually dimorphic manner. Mouse pituitary cells from the proopiomelanocortin lineage nearly completely lack NF68 immunoreactivity. PMID: 16940710 Alpha-internexin coassembles with all 3 neurofilament proteins into a single network of filaments in quadruple-transfected cells. PMID: 17005864 NFL gene deficiency could retard MSCs proliferation and neuronal generation, even though the capability of neuronal lineage differentiation of MSCs may not be deterred. PMID: 17395374 Disruption of neurofilament network with aggregation of NFL is a common triggering event of motor neuron degeneration in Charcot-Marie-Tooth disease. PMID: 17881652 Results suggest a preferential participation of P/Q-type Ca(2+) channels and hence alpha 1A subunits, in regulating spontaneous Ca(2+) transients in anterior pituitary cells under conditions where the proportion of NF68-expressing cells is high. PMID: 17927665 Results suggests that acrolein-mediated NF-L aggregation might be closely related to oxidative reactions, thus these reactions may play a critical role in neurodegenerative diseases. PMID: 18823586 LANP directly regulates expression of the neurofilament light chain, an important neuron-specific cytoskeletal gene, by binding to the promoter of this gene and modulating histone acetylation levels PMID: 19136565 These results support that TDP-43 is involved in neurofilament mRNA metabolism and transport, and provide insight into the pathogenesis of motor neuron death in ALS in which NFL mRNA levels are selectively suppressed. PMID: 19619516

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.